Intracellular Protein Degradation in Mammalian and Bacterial Cells

Figure 1: Core components of the Hippo pathway in mammalian cells. The Hippo pathway activity controls the dynamic localization of YAP/TAZ between nucleus and cytoplasm. (a) When the Hippo pathway is ...

Figure 2: Mechanical cues regulate YAP/TAZ activities through Rho GTPase and the Hippo pathway. Cell–cell contact, cell stretching, cell tension, extracellular matrix (ECM) stiffness, and changes in c...

Figure 3: The Hippo pathway integrates multiple signals to regulate the activity of YAP/TAZ. The LATS kinase activity is controlled by cell polarity and cell adhesion through KIBRA/NF2, tight junction...

Figure 4: YAP/TAZ and cancer hallmarks. The Hippo pathway effectors YAP/TAZ directly or indirectly control multiple cancer hallmarks, including proliferation, survival, evading growth suppressors, rep...

Figure 1: CRISPR-associated protein 9 (Cas9)-mediated sequence-specific genomic editing. (a) Comparison of programmable sequence-specific genome editing nucleases. (Top) Zinc-finger nucleases (ZFNs) a...

Figure 2: Nuclease-deactivated Cas9 (dCas9)-mediated sequence-specific gene regulation. (a) CRISPR interference (CRISPRi) strategies. Repression can occur with dCas9 alone in bacteria, which stericall...

Figure 3: Applications of CRISPR-associated protein 9 (Cas9) in gene editing, gene regulation, epigenome editing, and genomic imaging. (a) Cas9-mediated site-specific genome editing has a variety of a...

Figure 1: Overview of the five major protein import pathways of mitochondria. Presequence-carrying preproteins are imported by the translocase of the outer mitochondrial membrane (TOM) and the presequ...

Figure 2: The presequence pathway into the mitochondrial inner membrane (IM) and matrix. The translocase of the outer membrane (TOM) consists of three receptor proteins, the channel-forming protein To...

Figure 3: Role of the oxidase assembly (OXA) translocase in protein sorting. Proteins synthesized by mitochondrial ribosomes are exported into the inner membrane (IM) by the OXA translocase; the ribos...

Figure 4: Carrier pathway into the inner membrane. The precursors of the hydrophobic metabolite carriers are synthesized without a cleavable presequence. The precursors are bound to cytosolic chaperon...

Figure 5: Mitochondrial intermembrane space import and assembly (MIA) machinery. Many intermembrane space (IMS) proteins contain characteristic cysteine motifs. The precursors are kept in a reduced an...

Figure 6: Biogenesis of β-barrel proteins of the outer mitochondrial membrane. The precursors of β-barrel proteins are initially imported by the translocase of the outer membrane (TOM), bind to small ...

Figure 7: The dual role of mitochondrial distribution and morphology protein 10 (Mdm10) in protein assembly and organelle contact sites. Mdm10 associates with the sorting and assembly machinery (SAM) ...

Figure 8: Multiple import pathways for integral α-helical proteins of the mitochondrial outer membrane. The precursors of proteins with an N-terminal signal anchor sequence are typically inserted into...

Figure 9: The mitochondrial contact site and cristae organizing system (MICOS) interacts with protein translocases. MICOS consists of two core subunits, Mic10 and Mic60. Mic10 forms large oligomers th...

Figure 1: Exosomes are heterogeneous in size, heterogeneous in composition, and enriched in membrane-associated, high-order oligomeric protein complexes. Although it is likely that no exosome contains...

Figure 2: Exosomes bud from endosome and plasma membranes. Exosome biogenesis occurs by three modes: () vesicle budding into discrete endosomes that mature into multivesicular bodies, which release ex...

Figure 1: GFP sequences. (Line 1) The wild-type (WT) gfp10 gene as originally cloned and sequenced by Prasher et al (10). (Line 2) A popular humanized version (EGFP, Clontech Laboratories, Palo Alto,...

Figure 2: Mechanism proposed by Cubitt et al (22) for the intramolecular biosynthesis of the GFP chromophore, with rate constants estimated for the Ser65 → Thr mutant by Reid & Flynn (23) and Heim et...

Figure 3: Stereoview of the three-dimensional structure of GFP (30), showing 11 β-strands forming a hollow cylinder through which is threaded a helix bearing the chromophore, shown in ball-and-stick ...

Figure 4: Amino acid side chains, main chain carbonyls and amides, and solvent waters in the immediate vicinity of the chromophore of S65T GFP (30). Side chains are labeled with the one-letter code f...

Figure 5: Fluorescence excitation and emission spectra (solid and dashed lines, respectively) for typical members of the six major classes of GFP mutants, together with the chromophore structures bel...

Figure 6: Location on the GFP crystal structure (30) of the most important sites that improve folding at 37°C. The amino acids shown in space-filling representation are the wild-type residues that ar...